CATH Domain 3chrA03

CATH Classification

Level	CATH Code	Description
	1	Mainly Alpha
	1.10	Orthogonal Bundle
	1.10.390	Neutral Protease; domain 2
	1.10.390.10	Neutral Protease Domain 2

Domain Context

CATH Clusters

Superfamily	Neutral Protease Domain 2
Functional Family	Leukotriene A(4) hydrolase

Enzyme Information

3.3.2.6

Leukotriene-A(4) hydrolase.

based on mapping to UniProt P09960

(7E,9E,11Z,14Z)-(5S,6S)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H(2)O = (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate.

-!- A bifunctional zinc metalloprotease that displays both epoxide hydrolase and aminopeptidase activities. -!- It preferentially cleaves tripeptides at an arginyl bond, with dipeptides and tetrapeptides being poorer substrates. -!- It also converts leukotriene A(4) into leukotriene B(4), unlike EC 3.2.2.10 which converts leukotriene A(4) into 5,6-dihydroxy- 7,9,11,14-eicosatetraenoic acid.

UniProtKB Entries (1)

P09960

LKHA4_HUMAN

Homo sapiens

Leukotriene A-4 hydrolase

PDB Structure

PDB	3CHR
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Synthesis of glutamic acid analogs as potent inhibitors of leukotriene A4 hydrolase. Kirkland, T.A., Adler, M., Bauman, J.G., Chen, M., Haeggstrom, J.Z., King, B., Kochanny, M.J., Liang, A.M., Mendoza, L., Phillips, G.B., Thunnissen, M., Trinh, L., Whitlow, M., Ye, B., Ye, H., Parkinson, J., Guilford, W.J. Bioorg.Med.Chem.